Fig. 4: Lsm12 functions in NAADP signaling via its Lsm domain. | Nature Communications

Fig. 4: Lsm12 functions in NAADP signaling via its Lsm domain.

From: Lsm12 is an NAADP receptor and a two-pore channel regulatory protein required for calcium mobilization from acidic organelles

Fig. 4

a Putative domain assignment and predicted 3D structural model for Lsm12 (GenBank: AAH44587.1). Region assignment: Lsm domain, residues 4–67; Linker, residues 68–84; putative AD domain, residues 85–170. The structure was drawn with a previously created model (https://swissmodel.expasy.org/repository/uniprot/Q3MHD2)42. b Averaged NAADP-induced changes in Ca2+ indicator fluorescence in Lsm12-KO cells transfection with Lsm12 WT and mutant constructs. c Specific binding between 32P-NAADP and FLAG-tagged Lsm12 WT and ΔLsm proteins that were transiently expressed in Lsm12-KO cells and immunoprecipitated by an anti-FLAG antibody. d Immunoblot of Lsm12 WT and mutants pulled down by immobilized NAADP. e Co-immunoprecipitation between TPC2 and Lsm12 mutants. f Co-immunoprecipitation between TPC2 and Lsm12 in the absence or presence of 100 µM NAADP. Exp expression. Data were presented as mean value ± SEM. Unpaired Student’s t-test (two-tailed) was used to calculate p values. **** is for p value ≤ 0.0001.

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